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Lecture 6 - Cytoskeleton ST

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17 views

Lecture 6 - Cytoskeleton ST

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minhph.23bi14469
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Part 6

The cytoskeleton
The cytoplasm of eukaryotic cells is in constant motion

Movement of organelles

Secretory vesicles leave the ER, fuse with In mitotic cells, chromosomes first align
Golgi near the centre of the cell, and are and then move to opposite sides of the cell
transported to the plasma membrane
Three images, from a video, show an axon from a living neuron. Three vesicles, marked by red, yellow, and
blue arrowheads, are followed over a 6-second interval. Two vesicles move toward the tip of the axon and
one moves toward the cell body. (Photos courtesy of Paul Forscher, Yale University.)

Movement of organelles and chromosomes to the right place, at the right


time, is accomplished by the cytoskeleton
The movements of motile cells

Within body (animal cells) Through the environment


(single celled organism or gametes)

The white blood cells that track and Sperm cells swim through fluid to reach
destroy bacterial invaders crawl their destination
across a surface
Cytoskeleton

 Function:

- Movement

- Transport

- Organization and structural support that define the shapes of all cells

 Composed of three major types of


structural proteins:

-Microtubules

-Intermediate filaments

-Actin
1. Microtubules

 The basic subunit that forms a microtubule is the protein tubulin (hollow
polymers of tubulin heterodimers)

 Each molecule of α- and β-tubulin binds


a molecule of guanosine triphosphate
(GTP), near the front of the tubulin

Microtubules are cut by katanin, a


protein named for the Japanese word for
sword

The three-dimensional structure of the tubulin heterodimer, the basic


building block of a microtubule. In purple and green colors are the
polypeptide backbones of the two protein subunits, and in blue are the two
molecules of GTP that are bound to each heterodimer. Note the similarity in
the structures of the two subunits and that they are arranged head to tail in
the complex. At the right is a schematic drawing that shows how the dimer
is represented in the figures in the chapter
Structure from Protein Data Bank 1TUB. E. Nogales, S. G. Wolf, and K.
H. Downing, Nature 391 (1998): 199-203.
1. Microtubules

The structure of a small segment of a microtubule.


The individual tubulin heterodimers are aligned end to end in straight protofilaments, and the
protofilaments are arranged side by side to form a hollow tube. All heterodimers have the same
orientation, with the β-subunit toward one end of the microtubule and the α-subunit toward
the other. At the top are electron micrographs of microtubules assembled from pure tubulin
1. Microtubules

Mitotic spindle

Form the core of motile structures: cilia and flagella

Microtubules and motor proteins are even used by viruses, such as HIV and adenovirus,
allowing the viruses to rapidly reach the nucleus and replicate

Treatment
1. Microtubules

Drugs that make microtubules more or less stable block


mitosis and are used to treat cancers
Taxol (paclitaxel) binds to microtubules and makes
them more stable by preventing tubulin subunits from
dissociating
 Used to treat ovarian and breast cancers
Colchicine: causing a cell’s microtubules to disappear

 Used to treat gout

Zoxamide, a fungicide, binds specifically to fungal tubulins


and prevents fungal growth

The structures of three small organic molecules that disrupt microtubule


assembly or disassembly. Paclitaxel (Taxol™) and colchicine are natural
products produced by specific plants (the Pacific yew tree and the meadow
saffron, respectively). Zoxamide™ is a manufactured molecule discovered
by screening a large collection of small molecules for those with the ability
to interfere with microtubules
Some kinesins associate through their
tail domains, forming bipolar motors
with two motor head domains at each
end. Such motors can simultaneously Possible ways to generate bidirectional movement of a
bind and move along two microtubules cargo along a microtubule
of opposite polarity
Some viruses hijack the cell’s motors and use them to
Cells have two families of molecular transport themselves to the nucleus of the cell; HIV is one
motors that move on microtubules: example of a virus that uses the cell’s trucking system
kinesins, which usually move toward
the plus ends of microtubules, and
dyneins, which move toward
microtubules’ minus ends
1. Microtubules

The microtubules in a fibroblast cell,


viewed after labeling them with a
fluorescent dye so that they appear
green. The microtubules are organized
around a point (red) near the center of
Microtubule organizing center (MTOC): the cell and extend throughout the
+Centrosome cytoplasm. Most microtubules are long
+Basal body enough to run from one part of the cell to
another. (Photo courtesy of Lynne
Cassimeris, Lehigh University.)
Cilia and flagella

Light and fluorescence images of Chlamydomonas reinhardtii, a unicellular alga. Two very
prominent flagella extend from the top of each cell. Microtubules are in red in the
fluorescence image, showing that flagella are microtubule-based structures

Each of these organelles is composed of a long bundle of microtubules surrounded by an


extension of the plasma membrane.
https://www.khanacademy.org/test-prep/mcat/cells/cytoskeleton/v/microtubules-2
2. Actin

Actin is a ubiquitous and essential protein found in all eukaryotic cells.

Highly conserved; 90% identical between species

Actins filaments make up microfilament

Microfilaments function

-maintain cell shape


-muscle contraction
-cytoplasmic streaming
-cell motility
-cell division (cytokinesis)
2. Actin

Actin monomers self-associate and polymerize


into filaments ∼8 nm in diameter

An actin filament resembles a double-stranded


string of beads that has a right-handed helical
twist

Dynamic: longer by actin polymerization, shorter by


actin depolymerization

Actin monomers assemble head-to-tail


into double-stranded, polar filaments.
3. Intermediate filament

Intermediate filaments, or nanofilaments, are major components of the


cytoplasmic and nuclear cytoskeletons, made of various type of protein

8–12 nm thick and form resilient networks in the cytoplasm and nucleus.

Essential to maintain correct tissue structure and function.

Structural support, resist mechanical stress

Defective intermediate filaments are the cause of many human diseases


3. Intermediate filament

Most intermediate filament genes in humans encode keratins, expressed in all different kinds
of epithelial tissues of the body

Mutations in keratins cause epithelial cell fragility, an inherited skin-blistering disorder,


namely EBS

The condition illustrated here is EBS, the first disorder linked to intermediate filament gene
mutations, caused by mutations in keratins K5 or K14. The main photo shows the characteristic
skin blistering caused by scratching, rubbing, or tight clothing. The inset shows a section through a
diagnostic skin biopsy taken after rubbing the skin surface with a pencil eraser: The basal layer of
epidermal keratinocytes has a fluid-filled blister due to rupturing of the cells

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